PP4P1_MACFA
ID PP4P1_MACFA Reviewed; 284 AA.
AC Q4R6W2;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Type 1 phosphatidylinositol 4,5-bisphosphate 4-phosphatase;
DE Short=Type 1 PtdIns-4,5-P2 4-Ptase;
DE EC=3.1.3.78 {ECO:0000250|UniProtKB:Q86T03};
DE AltName: Full=PtdIns-4,5-P2 4-Ptase I;
DE AltName: Full=Transmembrane protein 55B;
GN Name=PIP4P1 {ECO:0000250|UniProtKB:Q86T03};
GN Synonyms=TMEM55B {ECO:0000250|UniProtKB:Q86T03}; ORFNames=QtsA-17009;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydrolysis of phosphatidylinositol-4,5-
CC bisphosphate (PtdIns-4,5-P2) to phosphatidylinositol-4-phosphate
CC (PtdIns-4-P) (By similarity). Does not hydrolyze phosphatidylinositol
CC 3,4,5-trisphosphate, phosphatidylinositol 3,4-bisphosphate, inositol
CC 3,5-bisphosphate, inositol 3,4-bisphosphate, phosphatidylinositol 5-
CC monophosphate, phosphatidylinositol 4-monophosphate and
CC phosphatidylinositol 3-monophosphate (By similarity). Regulates
CC lysosomal positioning by recruiting JIP4 to lysosomal membranes, thus
CC inducing retrograde transport of lysosomes along microtubules (By
CC similarity). Contributes to assembly of the V-ATPase complex in lipid
CC rafts of the lysosomal membrane and to subsequent amino acid-dependent
CC activation of mTORC1 (By similarity). May play a role in the regulation
CC of cellular cholesterol metabolism (By similarity).
CC {ECO:0000250|UniProtKB:Q86T03}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:25674,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57795,
CC ChEBI:CHEBI:58456; EC=3.1.3.78;
CC Evidence={ECO:0000250|UniProtKB:Q86T03};
CC -!- SUBUNIT: Interacts (via transmembrane domain) with ATP6V0D1 (By
CC similarity). Interacts with LAMTOR1, RRAGA and RRAGC (By similarity).
CC {ECO:0000250|UniProtKB:Q3TWL2}.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000250|UniProtKB:Q3TWL2}; Multi-pass membrane protein
CC {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q3TWL2}; Multi-
CC pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome
CC membrane {ECO:0000250|UniProtKB:Q3TWL2}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q3TWL2}; Multi-pass
CC membrane protein {ECO:0000255}.
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DR EMBL; AB169068; BAE01162.1; -; mRNA.
DR RefSeq; NP_001270945.1; NM_001284016.1.
DR RefSeq; XP_015308695.1; XM_015453209.1.
DR AlphaFoldDB; Q4R6W2; -.
DR STRING; 9541.XP_005560750.1; -.
DR GeneID; 101866619; -.
DR KEGG; mcf:101866619; -.
DR CTD; 90809; -.
DR eggNOG; KOG4684; Eukaryota.
DR OrthoDB; 1346704at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0030670; C:phagocytic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0034597; F:phosphatidylinositol-4,5-bisphosphate 4-phosphatase activity; IEA:InterPro.
DR GO; GO:0008203; P:cholesterol metabolic process; ISS:UniProtKB.
DR GO; GO:0032418; P:lysosome localization; ISS:UniProtKB.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; ISS:UniProtKB.
DR GO; GO:0070070; P:proton-transporting V-type ATPase complex assembly; ISS:UniProtKB.
DR GO; GO:0006991; P:response to sterol depletion; ISS:UniProtKB.
DR InterPro; IPR019178; PtdIns-P2-Ptase.
DR PANTHER; PTHR21014; PTHR21014; 1.
DR Pfam; PF09788; Tmemb_55A; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasmic vesicle; Endosome; Hydrolase; Lipid metabolism;
KW Lysosome; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..284
FT /note="Type 1 phosphatidylinositol 4,5-bisphosphate 4-
FT phosphatase"
FT /id="PRO_0000235233"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 140..146
FT /note="CX5R motif"
FT COMPBIAS 46..80
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 140
FT /evidence="ECO:0000250"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3TWL2"
SQ SEQUENCE 284 AA; 30185 MW; 7EA24D2735640FDF CRC64;
MAADGERSPL LSEPIDGGAG GNGLVGPGGS GAGPGGGLTP SAPPYGAGKH APPQAFPPFP
EGHPAVLPGE DPPPYSPLTS PDSGSAPMIT CRVCQSLINV EGKMHQHVVK CGVCNEATPI
KNAPPGKKYV RCPCNCLLIC KVTSQRIACP RPYCKRIINL GPVHPGPLSP EPQPMGVRVI
CGHCKNTFLW TEFTDRTLAR CPHCRKVSSI GRRYPRKRCI CCFLLGLLLA VTATGLAFGT
WKHARRYGGI YAAWAFVILL AVLCLGRALY WACMKVSHPV QNFS
